High performance research tools for cell and protein isolationRudolf-Wissell-Str. 28
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IBA Lifesciences GmbH – Solutions for Life SciencesIBA Lifesciences GmbH is a biotechnology company providing products for life science research in academia and industry. We develop high performance research tools for cell and protein isolation based on our proprietary Strep-tag® technology. Headquartered in Göttingen, Germany, we have built a network of worldwide distributors, making our products available in over 40 countries across 5 continents.
Strep-tag® technologyThe Strep-tag® technology exploits on one of the strongest non-covalent interactions in nature: the interaction of biotin and streptavidin. Strep-tag® II and its tandem equivalent Twin-Strep-tag® are peptide sequences exhibiting intrinsic affinity towards the biotin-binding pocket of two specifically engineered streptavidin variants, Strep-Tactin® and its high affinity version Strep-Tactin®XT. The range of selectable affinities as well as the reversibility of the binding interaction makes the Strep-tag® system a universal tool for isolation of proteins, cells, and exosomes.
Strep-tag® technology in protein purification and analysis
The Strep-tag® system enables cloning, expression, detection, purification, and immobilization of recombinant proteins. The highly specific interaction of the Strep-tag® with Strep-Tactin® ensures efficient one-step purification of the protein of interest and isolation of Strep-tagged targets even from crude cell lysate in unparalleled purity. The mild and physiological conditions promote the yield of fully functional proteins, making the system particularly suitable for purification of enzymes as well as structural investigations, protein-protein interaction studies, ligand-receptor investigations, or even separation of living cells for re-culturing processes. The Strep-tag® technology is compatible with a large number of protein classes, e.g. metalloproteins, membrane proteins, and fragile protein complexes with multiple subunits. Simultaneously, a high tolerance towards different buffers and additives promotes its universal applicability. The near covalent affinity (pM range) of Twin-Strep-tag® to Strep-Tactin®XT expands the range of applications of the Strep-tag® system towards protein analysis e. g. SPR analysis or bio-layer interferometry (BLI).
Strep-tag® technology for cell isolation, expansion and staining
Our Strep-tag® technology is also applicable to various cellular research approaches. Cell isolations should aim at keeping the cells in their natural state. Due to the reversible binding properties of the Strep-tag® technology, it is an ideal tool to capture and release cells with minimal impact. The technology is applicable to isolating and/or staining cells according to their surface markers (Fab-TACS®/Nano-TACS® approach) or based on their antigen-specificity (MHC I Streptamer® approach). The selection reagents bind loosely to the cells and are therefore easily removable. This principle is very similar in all our cell isolation and staining approaches.
For different analyses and further experiments it is necessary to expand cells in numbers. Our CD3/CD28 Streptamer® approach addresses this requirement and offers full removability from the cells after initial activation and stimulation. All Strep-tag® products available for cell research aim at preserving the authentic properties, full effector function as well as viability of the target cells.
Strep-tag® technology for exosome isolation
The Strep-tag® technology is also applicable for isolation of exosomes. Targeting exosomes surface markers with low affinity Fab fragments allows quick, simple, and highly pure isolation of these small particles from different sources such as cell culture media, serum, or plasma.
PeopleDr Mike Rothe (Chief Executive Officer)
Dr Joachim Bertram (Chief Scientific Officer)
Dr Herbert Stadler (Head of the Advisory Board)
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Ansprechpersonen bei IBA GmbH:
Frau Anna Färger
Karrierechancen und StellenangeboteIBA GmbH
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High performance research tools for cell and protein isolation